Functional, structural properties and interaction mechanism of soy protein isolate nanoparticles modified by high-performance protein-glutaminase. (May 2023)
- Record Type:
- Journal Article
- Title:
- Functional, structural properties and interaction mechanism of soy protein isolate nanoparticles modified by high-performance protein-glutaminase. (May 2023)
- Main Title:
- Functional, structural properties and interaction mechanism of soy protein isolate nanoparticles modified by high-performance protein-glutaminase
- Authors:
- Zheng, Nan
Long, Mengfei
Zhang, Zehua
Osire, Tolbert
Zan, Qijia
Zhou, Huimin
Du, Shuang
Xia, Xiaole - Abstract:
- Abstract: Investigating the changes in the structural and functional properties of soy protein isolate (SPI) modified by high-performance protein-glutaminase (PG) and understanding their interactions are crucial for the application of SPI nanoparticles. Herein, the thermal stability and activity of PG were evolved by computer-assisted rational design strategy, generating the best variant Z15 (N16M/N20L/Q21H/K48R/S81E/T113E) with a 4.65-fold improved activity (75.57 U/mg) and increased thermal stability (Δ T m = 4.6 °C), one of the best performing PG. SPI treated with Z15 showed better solubility, foaming, and emulsifying properties than the wild type PG-deamidation, which were increased by 1.25-fold, 45.45%, and 38.95%, respectively. Furthermore, SPI treated with Z15 exhibited lower hardness and higher cohesiveness. By systematically analyzing the structural characteristics, SPI nanoparticles possessed a coarse, loose, and porous microstructure. Molecular dynamics simulations suggested that the Glu81 and Glu113 residues of Z15 contributed the most to the stabilization interaction in β-conglycinin-Z15 complexes. These results could provide theoretical guidance for the potential application of SPI nanoparticles in sustainable green plant-based foods industries. Graphical abstract: Image 1 Highlights: Z15 exhibited great specific activity (75.57 U/mg) and thermostability ( T m 72.4 °C). SPI nanoparticles treated with Z15 showed dramatic increase in functional properties. SPIAbstract: Investigating the changes in the structural and functional properties of soy protein isolate (SPI) modified by high-performance protein-glutaminase (PG) and understanding their interactions are crucial for the application of SPI nanoparticles. Herein, the thermal stability and activity of PG were evolved by computer-assisted rational design strategy, generating the best variant Z15 (N16M/N20L/Q21H/K48R/S81E/T113E) with a 4.65-fold improved activity (75.57 U/mg) and increased thermal stability (Δ T m = 4.6 °C), one of the best performing PG. SPI treated with Z15 showed better solubility, foaming, and emulsifying properties than the wild type PG-deamidation, which were increased by 1.25-fold, 45.45%, and 38.95%, respectively. Furthermore, SPI treated with Z15 exhibited lower hardness and higher cohesiveness. By systematically analyzing the structural characteristics, SPI nanoparticles possessed a coarse, loose, and porous microstructure. Molecular dynamics simulations suggested that the Glu81 and Glu113 residues of Z15 contributed the most to the stabilization interaction in β-conglycinin-Z15 complexes. These results could provide theoretical guidance for the potential application of SPI nanoparticles in sustainable green plant-based foods industries. Graphical abstract: Image 1 Highlights: Z15 exhibited great specific activity (75.57 U/mg) and thermostability ( T m 72.4 °C). SPI nanoparticles treated with Z15 showed dramatic increase in functional properties. SPI nanoparticles treated with Z15 presented excellent homogeneity and stability. Glu81 and Glu113 were key residues with big energy contribution in 7S-Z15 complexes. … (more)
- Is Part Of:
- Food hydrocolloids. Volume 139(2023)
- Journal:
- Food hydrocolloids
- Issue:
- Volume 139(2023)
- Issue Display:
- Volume 139, Issue 2023 (2023)
- Year:
- 2023
- Volume:
- 139
- Issue:
- 2023
- Issue Sort Value:
- 2023-0139-2023-0000
- Page Start:
- Page End:
- Publication Date:
- 2023-05
- Subjects:
- Soy protein isolate nanoparticles -- Protein-glutaminase -- Protein-protein interaction -- Molecular dynamics simulation -- Functional properties -- Structural characteristics
Hydrocolloids -- Periodicals
Food additives -- Periodicals
Colloïdes -- Périodiques
Aliments -- Additifs -- Périodiques
Colloids
Food additives
Periodicals
Electronic journals
664.06 - Journal URLs:
- http://www.sciencedirect.com/science/journal/0268005X ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodhyd.2023.108594 ↗
- Languages:
- English
- ISSNs:
- 0268-005X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.556000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 26090.xml